Virus membrane fusion
Identifieur interne : 000935 ( Pmc/Checkpoint ); précédent : 000934; suivant : 000936Virus membrane fusion
Auteurs : Winfried Weissenhorn [France] ; Andreas Hinz [France] ; Yves Gaudin [France]Source :
- Febs Letters [ 0014-5793 ] ; 2007.
Abstract
Membrane fusion of enveloped viruses with cellular membranes is mediated by viral glycoproteins (GP). Interaction of GP with cellular receptors alone or coupled to exposure to the acidic environment of endosomes induces extensive conformational changes in the fusion protein which pull two membranes into close enough proximity to trigger bilayer fusion. The refolding process provides the energy for fusion and repositions both membrane anchors, the transmembrane and the fusion peptide regions, at the same end of an elongated hairpin structure in all fusion protein structures known to date. The fusion process follows several lipidic intermediate states, which are generated by the refolding process. Although the major principles of viral fusion are understood, the structures of fusion protein intermediates and their mode of lipid bilayer interaction, the structures and functions of the membrane anchors and the number of fusion proteins required for fusion, necessitate further investigations.
Url:
DOI: 10.1016/j.febslet.2007.01.093
PubMed: 17320081
PubMed Central: 7094569
Affiliations:
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sort="Weissenhorn, Winfried" uniqKey="Weissenhorn W" first="Winfried" last="Weissenhorn">Winfried Weissenhorn</name><affiliation wicri:level="3"><nlm:aff id="aff1">European Molecular Biology Laboratory, 6 Rue Jules Horowitz, 38042 Grenoble, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>European Molecular Biology Laboratory, 6 Rue Jules Horowitz, 38042 Grenoble</wicri:regionArea><placeName><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Rhône-Alpes</region><settlement type="city">Grenoble</settlement></placeName></affiliation></author><author><name sortKey="Hinz, Andreas" sort="Hinz, Andreas" uniqKey="Hinz A" first="Andreas" last="Hinz">Andreas Hinz</name><affiliation wicri:level="3"><nlm:aff id="aff1">European Molecular Biology Laboratory, 6 Rue Jules Horowitz, 38042 Grenoble, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>European Molecular Biology Laboratory, 6 Rue Jules Horowitz, 38042 Grenoble</wicri:regionArea><placeName><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Rhône-Alpes</region><settlement type="city">Grenoble</settlement></placeName></affiliation></author><author><name sortKey="Gaudin, Yves" sort="Gaudin, Yves" uniqKey="Gaudin Y" first="Yves" last="Gaudin">Yves Gaudin</name><affiliation wicri:level="3"><nlm:aff id="aff2">CNRS, UMR2472, INRA, UMR1157, IFR115, Laboratoire de Virologie Moléculaire et Structurale, 91198, Gif sur Yvette, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>CNRS, UMR2472, INRA, UMR1157, IFR115, Laboratoire de Virologie Moléculaire et Structurale, 91198, Gif sur Yvette</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Gif-sur-Yvette</settlement></placeName></affiliation></author></analytic><series><title level="j">Febs Letters</title><idno type="ISSN">0014-5793</idno><idno type="eISSN">1873-3468</idno><imprint><date when="2007">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Membrane fusion of enveloped viruses with cellular membranes is mediated by viral glycoproteins (GP). Interaction of GP with cellular receptors alone or coupled to exposure to the acidic environment of endosomes induces extensive conformational changes in the fusion protein which pull two membranes into close enough proximity to trigger bilayer fusion. The refolding process provides the energy for fusion and repositions both membrane anchors, the transmembrane and the fusion peptide regions, at the same end of an elongated hairpin structure in all fusion protein structures known to date. The fusion process follows several lipidic intermediate states, which are generated by the refolding process. Although the major principles of viral fusion are understood, the structures of fusion protein intermediates and their mode of lipid bilayer interaction, the structures and functions of the membrane anchors and the number of fusion proteins required for fusion, necessitate further investigations.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Skehel, J J" uniqKey="Skehel J">J.J. Skehel</name></author><author><name sortKey="Wiley, D C" uniqKey="Wiley D">D.C. Wiley</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Harrison, S C" uniqKey="Harrison S">S.C. Harrison</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kielian, M" uniqKey="Kielian M">M. Kielian</name></author><author><name sortKey="Rey, F A" uniqKey="Rey F">F.A. Rey</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lamb, R A" uniqKey="Lamb R">R.A. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">FEBS Lett</journal-id><journal-id journal-id-type="iso-abbrev">FEBS Lett</journal-id><journal-title-group><journal-title>Febs Letters</journal-title></journal-title-group><issn pub-type="ppub">0014-5793</issn><issn pub-type="epub">1873-3468</issn><publisher><publisher-name>John Wiley & Sons Ltd</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">17320081</article-id><article-id pub-id-type="pmc">7094569</article-id><article-id pub-id-type="publisher-id">S0014-5793(07)00166-4</article-id><article-id pub-id-type="doi">10.1016/j.febslet.2007.01.093</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Virus membrane fusion</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Weissenhorn</surname><given-names>Winfried</given-names></name><email>weissenhorn@embl.fr</email><xref rid="aff1" ref-type="aff">a</xref><xref rid="cor1" ref-type="corresp">⁎</xref><xref rid="fn1" ref-type="fn">1</xref></contrib><contrib contrib-type="author"><name><surname>Hinz</surname><given-names>Andreas</given-names></name><xref rid="aff1" ref-type="aff">a</xref><xref rid="fn1" ref-type="fn">1</xref></contrib><contrib contrib-type="author"><name><surname>Gaudin</surname><given-names>Yves</given-names></name><email>gaudin@vms.cnrs-gif.fr</email><xref rid="aff2" ref-type="aff">b</xref></contrib></contrib-group><aff id="aff1"><label>a</label>European Molecular Biology Laboratory, 6 Rue Jules Horowitz, 38042 Grenoble, France</aff><aff id="aff2"><label>b</label>CNRS, UMR2472, INRA, UMR1157, IFR115, Laboratoire de Virologie Moléculaire et Structurale, 91198, Gif sur Yvette, France</aff><author-notes><corresp id="cor1"><label>⁎</label>Corresponding author. <email>weissenhorn@embl.fr</email></corresp><fn id="fn1"><label>1</label><p>Present address: University Joseph Fourier, Unit of Virus Host Cell Interactions (UVHCI), UMR 5233 UJF-EMBL-CNRS, 6 Rue Jules Horowitz 38042, 30042 Grenoble, France.</p></fn></author-notes><pub-date pub-type="pmc-release"><day>16</day><month>2</month><year>2007</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><day>22</day><month>5</month><year>2007</year></pub-date><pub-date pub-type="epub"><day>16</day><month>2</month><year>2007</year></pub-date><volume>581</volume><issue>11</issue><fpage>2150</fpage><lpage>2155</lpage><history><date date-type="received"><day>11</day><month>12</month><year>2006</year></date><date date-type="accepted"><day>18</day><month>1</month><year>2007</year></date></history><permissions><copyright-statement>Copyright © 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</copyright-statement><copyright-year>2007</copyright-year><copyright-holder>Federation of European Biochemical Societies</copyright-holder><license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p></license></permissions><abstract><p>Membrane fusion of enveloped viruses with cellular membranes is mediated by viral glycoproteins (GP). Interaction of GP with cellular receptors alone or coupled to exposure to the acidic environment of endosomes induces extensive conformational changes in the fusion protein which pull two membranes into close enough proximity to trigger bilayer fusion. The refolding process provides the energy for fusion and repositions both membrane anchors, the transmembrane and the fusion peptide regions, at the same end of an elongated hairpin structure in all fusion protein structures known to date. The fusion process follows several lipidic intermediate states, which are generated by the refolding process. Although the major principles of viral fusion are understood, the structures of fusion protein intermediates and their mode of lipid bilayer interaction, the structures and functions of the membrane anchors and the number of fusion proteins required for fusion, necessitate further investigations.</p></abstract><kwd-group><title>Keywords</title><kwd>Membrane fusion</kwd><kwd>Hemifusion</kwd><kwd>Influenza virus hemagglutinin</kwd><kwd>HIV-1 gp41</kwd><kwd>Paramyxovirus F</kwd><kwd>SFV E1</kwd><kwd>TBE E</kwd><kwd>VSV G</kwd><kwd>Herpes simplex virus gB</kwd><kwd>Class I, II, III membrane fusion protein</kwd></kwd-group></article-meta></front></pmc><affiliations><list><country><li>France</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Rhône-Alpes</li><li>Île-de-France</li></region><settlement><li>Gif-sur-Yvette</li><li>Grenoble</li></settlement></list><tree><country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Weissenhorn, Winfried" sort="Weissenhorn, Winfried" uniqKey="Weissenhorn W" first="Winfried" last="Weissenhorn">Winfried Weissenhorn</name></region><name sortKey="Gaudin, Yves" sort="Gaudin, Yves" uniqKey="Gaudin Y" first="Yves" last="Gaudin">Yves Gaudin</name><name sortKey="Hinz, Andreas" sort="Hinz, Andreas" uniqKey="Hinz A" first="Andreas" last="Hinz">Andreas Hinz</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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